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3L9N

crystal structure of PKAB3 (pka triple mutant V123A, L173M, Q181K) with compound 27

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001669cellular_componentacrosomal vesicle
A0001707biological_processmesoderm formation
A0001843biological_processneural tube closure
A0002027biological_processregulation of heart rate
A0003091biological_processrenal water homeostasis
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004679molecular_functionAMP-activated protein kinase activity
A0004691molecular_functioncAMP-dependent protein kinase activity
A0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005930cellular_componentaxoneme
A0005952cellular_componentcAMP-dependent protein kinase complex
A0006397biological_processmRNA processing
A0006468biological_processprotein phosphorylation
A0006611biological_processprotein export from nucleus
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0010737biological_processprotein kinase A signaling
A0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
A0016241biological_processregulation of macroautophagy
A0016310biological_processphosphorylation
A0016607cellular_componentnuclear speck
A0018105biological_processpeptidyl-serine phosphorylation
A0019221biological_processcytokine-mediated signaling pathway
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0030145molecular_functionmanganese ion binding
A0031410cellular_componentcytoplasmic vesicle
A0031514cellular_componentmotile cilium
A0031594cellular_componentneuromuscular junction
A0031625molecular_functionubiquitin protein ligase binding
A0032024biological_processpositive regulation of insulin secretion
A0032703biological_processnegative regulation of interleukin-2 production
A0034237molecular_functionprotein kinase A regulatory subunit binding
A0034380biological_processhigh-density lipoprotein particle assembly
A0034605biological_processcellular response to heat
A0034704cellular_componentcalcium channel complex
A0035694biological_processmitochondrial protein catabolic process
A0036126cellular_componentsperm flagellum
A0044853cellular_componentplasma membrane raft
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0045667biological_processregulation of osteoblast differentiation
A0045722biological_processpositive regulation of gluconeogenesis
A0045879biological_processnegative regulation of smoothened signaling pathway
A0046827biological_processpositive regulation of protein export from nucleus
A0048240biological_processsperm capacitation
A0048471cellular_componentperinuclear region of cytoplasm
A0050804biological_processmodulation of chemical synaptic transmission
A0050850biological_processpositive regulation of calcium-mediated signaling
A0051726biological_processregulation of cell cycle
A0055117biological_processregulation of cardiac muscle contraction
A0061136biological_processregulation of proteasomal protein catabolic process
A0070062cellular_componentextracellular exosome
A0070417biological_processcellular response to cold
A0070613biological_processregulation of protein processing
A0071333biological_processcellular response to glucose stimulus
A0071374biological_processcellular response to parathyroid hormone stimulus
A0071377biological_processcellular response to glucagon stimulus
A0071872biological_processcellular response to epinephrine stimulus
A0086064biological_processcell communication by electrical coupling involved in cardiac conduction
A0097546cellular_componentciliary base
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0099103molecular_functionchannel activator activity
A0099170biological_processpostsynaptic modulation of chemical synaptic transmission
A0106310molecular_functionprotein serine kinase activity
A1903779biological_processregulation of cardiac conduction
A1904262biological_processnegative regulation of TORC1 signaling
A1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
A1990044biological_processprotein localization to lipid droplet
A2000810biological_processregulation of bicellular tight junction assembly
C0004862molecular_functioncAMP-dependent protein kinase inhibitor activity
C0006469biological_processnegative regulation of protein kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE L9N A 351
ChainResidue
ALEU49
AASN171
AMET173
ATHR183
AASP184
AHOH394
AHOH411
AHOH485
AHOH506
APHE54
AALA70
ALYS72
AMET120
AGLU121
AALA123
AGLU127
AGLU170

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhketgnh..........YAMK
ChainResidueDetails
ALEU49-LYS72

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLMI
ChainResidueDetails
ALEU162-ILE174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsSITE: Important for inhibition => ECO:0000250
ChainResidueDetails
CARG15
CARG18
CARG19

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALEU49

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS72
AGLU121
ALYS168

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Deamidated asparagine => ECO:0000250|UniProtKB:P05132
ChainResidueDetails
AASN2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132
ChainResidueDetails
ASER10

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
ATHR48

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05132
ChainResidueDetails
ASER139

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:12372837
ChainResidueDetails
ATHR195

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:12372837, ECO:0000269|PubMed:16765046, ECO:0000269|PubMed:20137943, ECO:0000269|PubMed:20481595, ECO:0000269|PubMed:20732331, ECO:0000269|PubMed:21774789, ECO:0000269|Ref.43
ChainResidueDetails
ATPO197

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05132
ChainResidueDetails
ATYR330

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:16765046, ECO:0000269|PubMed:20137943, ECO:0000269|PubMed:20481595, ECO:0000269|PubMed:20732331, ECO:0000269|PubMed:21774789, ECO:0000269|Ref.43, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASEP338

site_idSWS_FT_FI12
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:25807930
ChainResidueDetails
AGLY1

226707

PDB entries from 2024-10-30

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